CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.70 | Cathepsin B; Chain A |
|
3.90.70.10 | Cysteine proteinases |
Domain Context
CATH Clusters
| Superfamily | Cysteine proteinases |
| Functional Family | Putative ubiquitin carboxyl-terminal hydrolase CYLD |
Enzyme Information
| 3.4.19.12 |
Ubiquitinyl hydrolase 1.
based on mapping to UniProt Q9NQC7
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
-!- Links to polypeptides smaller than 60 residues are hydrolyzed more readily than those to larger polypeptides. -!- Isoforms exist with quantitatively different specificities among the best known being UCH-L1 and UCH-L3, major proteins of the brain of mammals. -!- Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde). -!- Belongs to peptidase family C12.
|
UniProtKB Entries (1)
| Q9NQC7 |
CYLD_HUMAN
Homo sapiens
Ubiquitin carboxyl-terminal hydrolase CYLD
|
PDB Structure
| PDB | 2VHF |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The Structure of the Cyld Usp Domain Explains its Specificity for Lys63-Linked Polyubiquitin and Reveals a B-Box Module
Mol.Cell.Biol.
|